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The Journal of Immunology, 1968, 100: 69-79.
Copyright © 1968 by The American Association of Immunologists, Inc.
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The Inhibition by Normal {gamma}G-Globulins of Antibodies Specific for Individual {gamma}G Myeloma Proteins1

Daniel Hurez, Gilbert Meshaka2, Constantin Mihaesco3 and Maxime Seligmann

Laboratory of Immunochemistry, Research Institute on Blood Diseases, Hôpital Saint-Louis, Paris, France

Abstract

Thirty-three antisera to ten isolated {gamma}G myeloma globulins were first absorbed in order to show only individual antigenic specificity of the homologous myeloma protein. Further absorption with variable but usually large amounts of normal fraction II resulted in the complete neutralization of the individually specific antibodies in 13 antisera. Absorption with as much as 100 mg/ml of fraction II resulted in partial neutralization of individually specific antibodies for 19 sera, whereas one antiserum was practically not affected. The ability of fraction II to neutralize individually specific antibodies varied greatly for the different kinds of antibodies to a given myeloma globulin, even within the same antiserum.

It was demonstrated that neutralization by normal {gamma}G-globulins of these antibodies to individual specific antigens was due to specific inhibition without precipitation. Inhibition curves showed that the molecular localization on normal {gamma}G-globulins of the antigenic structures involved in this inhibition phenomenon is similar to that of the individual specific antigens on the homologous myeloma globulin.

These findings are discussed in view of the analogy of myeloma globulins to their normal counterparts and to purified antibodies.

Footnotes

These studies were supported in part by Grant CR.66.237. of French National Institute for Medical Research.

2 Chargé de Recherches à l'I.N.S.E.R.M.

3 Maître de Recherches à l'I.N.S.E.R.M.






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